ID   DHET_ACEEU              Reviewed;         739 AA.
AC   Q44002; O07952;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 75.
DE   RecName: Full=Alcohol dehydrogenase [acceptor];
DE            EC=1.1.99.8;
DE   Flags: Precursor;
GN   Name=adh;
OS   Acetobacter europaeus (Gluconacetobacter europaeus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=33995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51845 / DSM 6160 / DES11 / LMG 18890;
RA   Thurner C.A.K.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: A primary alcohol + acceptor = an aldehyde +
CC       reduced acceptor.
CC   -!- COFACTOR: Binds 1 PQQ group per subunit. PQQ is inserted between
CC       disulfide Cys-143-Cys-144 and the indole ring of Trp-281 (By
CC       similarity).
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 heme group per subunit (By similarity).
CC   -!- SUBUNIT: Heterotetramer (dehydrogenase, cytochrome, and two
CC       smaller unknown subunits) that forms the alcohol dehydrogenase
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Periplasmic side (Potential).
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 cytochrome c domain.
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DR   EMBL; X82894; CAA58066.1; -; Genomic_DNA.
DR   EMBL; Y09480; CAA70688.1; -; Genomic_DNA.
DR   HSSP; Q46444; 1KB0.
DR   BRENDA; 1.1.99.8; 264198.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0018468; F:alcohol dehydrogenase (acceptor) activity; IEA:EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR019556; PQQ-dependent_C.
DR   InterPro; IPR019551; PQQ-dependent_N.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR001479; Quinoprotein_DH_CS.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1.
DR   Pfam; PF01011; PQQ; 6.
DR   Pfam; PF10535; PQQ_C; 1.
DR   Pfam; PF10527; PQQ_N; 1.
DR   SMART; SM00564; PQQ; 5.
DR   TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR   PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Calcium; Cell membrane; Disulfide bond; Heme; Iron; Membrane;
KW   Metal-binding; Oxidoreductase; PQQ; Signal.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    739       Alcohol dehydrogenase [acceptor].
FT                                /FTId=PRO_0000025560.
FT   DOMAIN      635    739       Cytochrome c.
FT   ACT_SITE    344    344       Proton acceptor (Potential).
FT   METAL       217    217       Calcium (By similarity).
FT   METAL       299    299       Calcium (By similarity).
FT   METAL       655    655       Iron (heme axial ligand) (By similarity).
FT   BINDING     651    651       Heme (covalent) (By similarity).
FT   BINDING     654    654       Heme (covalent) (By similarity).
FT   DISULFID    143    144       By similarity.
SQ   SEQUENCE   739 AA;  80945 MW;  E681BB237ACB91F4 CRC64;
     MISAVFGKRR SLSRTLTAGT ICAALISGYA TMASADDGQG ATGEAIIHAD DHPGNWMTYG
     RTYSEQRYSP LDQINRSNVG NLKLAWYLDL DTNRGQEGTP LVIDGVMYAT TNWSMMKAVD
     AATGKLLWSY DPRVPGNIAD KGCCDTVNRG AAYWNGKVYF GTFDGRLIAL DAKTGKLVWS
     VNTIPPEAEL GKQRSYTVDG APRIAKGRVI IGNGGSEFGA RGFVTAFDAE TGKVDWRFFT
     APNPKNEPDH TASDSVLMNK AYQTWSPTGA WTRQGGGGTV WDSIVYDPVA DLVYLGVGNG
     SPWNYKYRSE GKGDNLFLGS IVALKPETGE YVWHFQETPM DQWDFTSVQQ IMTLDLPING
     ETRHVIVHAP KNGFFYIIDA KTGEFISGKN YVYVNWASGL DPKTGRPIYN PDALYTLTGK
     EWYGIPGDLG GHNFAAMAFS PKTGLVYIPA QQVPFLYTNQ VGGFTPHPDS WNLGLDMNKV
     GIPDSPEAKQ AFVKDLKGWI VAWDPQKQAE AWRVDHKGPW NGGILATGGD LLFQGLANGE
     FHAYDATNGS DLFHFAADSG IIAPPVTYLA NGKQYVAVEV GWGGIYPFFL GGLARTSGWT
     VNHSRIIAFS LDGKSGPLPK QNDQGFLPVK PPAQFDSKRT DNGYFQFQTY CAACHGDNAE
     GAGVLPDLRW SGSIRHEDAF YNVVGRGALT AYGMDRFDGN MNPTEIEDIR QFLIKRANET
     YQREVDARKN ADGIPEQLP
//